PMID- 20844028
OWN - NLM
STAT- MEDLINE
DCOM- 20101122
LR  - 20221207
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 84
IP  - 22
DP  - 2010 Nov
TI  - Novel immunodominant peptide presentation strategy: a featured 
      HLA-A*2402-restricted cytotoxic T-lymphocyte epitope stabilized by intrachain 
      hydrogen bonds from severe acute respiratory syndrome coronavirus nucleocapsid 
      protein.
PG  - 11849-57
LID - 10.1128/JVI.01464-10 [doi]
AB  - Antigenic peptides recognized by virus-specific cytotoxic T lymphocytes (CTLs) 
      are presented by major histocompatibility complex (MHC; or human leukocyte 
      antigen [HLA] in humans) molecules, and the peptide selection and presentation 
      strategy of the host has been studied to guide our understanding of cellular 
      immunity and vaccine development. Here, a severe acute respiratory syndrome 
      coronavirus (SARS-CoV) nucleocapsid (N) protein-derived CTL epitope, N1 
      (QFKDNVILL), restricted by HLA-A*2402 was identified by a series of in vitro 
      studies, including a computer-assisted algorithm for prediction, stabilization of 
      the peptide by co-refolding with HLA-A*2402 heavy chain and beta(2)-microglobulin 
      (beta(2)m), and T2-A24 cell binding. Consequently, the antigenicity of the peptide 
      was confirmed by enzyme-linked immunospot (ELISPOT), proliferation assays, and 
      HLA-peptide complex tetramer staining using peripheral blood mononuclear cells 
      (PBMCs) from donors who had recovered from SARS donors. Furthermore, the crystal 
      structure of HLA-A*2402 complexed with peptide N1 was determined, and the 
      featured peptide was characterized with two unexpected intrachain hydrogen bonds 
      which augment the central residues to bulge out of the binding groove. This may 
      contribute to the T-cell receptor (TCR) interaction, showing a host 
      immunodominant peptide presentation strategy. Meanwhile, a rapid and efficient 
      strategy is presented for the determination of naturally presented CTL epitopes 
      in the context of given HLA alleles of interest from long immunogenic overlapping 
      peptides.
FAU - Liu, Jun
AU  - Liu J
AD  - Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's 
      Republic of China.
FAU - Wu, Peng
AU  - Wu P
FAU - Gao, Feng
AU  - Gao F
FAU - Qi, Jianxun
AU  - Qi J
FAU - Kawana-Tachikawa, Ai
AU  - Kawana-Tachikawa A
FAU - Xie, Jing
AU  - Xie J
FAU - Vavricka, Christopher J
AU  - Vavricka CJ
FAU - Iwamoto, Aikichi
AU  - Iwamoto A
FAU - Li, Taisheng
AU  - Li T
FAU - Gao, George F
AU  - Gao GF
LA  - eng
SI  - PDB/3I6L
PT  - Evaluation Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100915
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Epitopes, T-Lymphocyte)
RN  - 0 (HLA-A Antigens)
RN  - 0 (Nucleocapsid Proteins)
RN  - 0 (Peptide Fragments)
SB  - IM
MH  - Adult
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Cell Line
MH  - Cells, Cultured
MH  - Epitope Mapping/*methods
MH  - Epitopes, T-Lymphocyte/*chemistry/genetics/*immunology
MH  - Female
MH  - HLA-A Antigens/*chemistry/genetics/immunology
MH  - Humans
MH  - Hydrogen Bonding
MH  - Leukocytes, Mononuclear/chemistry/immunology/virology
MH  - Male
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nucleocapsid Proteins/*chemistry/genetics/*immunology
MH  - Peptide Fragments/chemistry/genetics/*immunology
MH  - Protein Folding
MH  - Severe acute respiratory syndrome-related 
      coronavirus/chemistry/genetics/*immunology
MH  - Severe Acute Respiratory Syndrome/*immunology/virology
MH  - T-Lymphocytes, Cytotoxic/chemistry/immunology
PMC - PMC2977860
EDAT- 2010/09/17 06:00
MHDA- 2010/12/14 06:00
PMCR- 2010/09/15
CRDT- 2010/09/17 06:00
PHST- 2010/09/17 06:00 [entrez]
PHST- 2010/09/17 06:00 [pubmed]
PHST- 2010/12/14 06:00 [medline]
PHST- 2010/09/15 00:00 [pmc-release]
AID - JVI.01464-10 [pii]
AID - 1464-10 [pii]
AID - 10.1128/JVI.01464-10 [doi]
PST - ppublish
SO  - J Virol. 2010 Nov;84(22):11849-57. doi: 10.1128/JVI.01464-10. Epub 2010 Sep 15.